Chemokine receptor CXCR4 oligomerization is disrupted selectively by the antagonist ligand IT1t.

ABSTRACT: CXCR4, a member of the family of chemokine-activated G protein-coupled receptors, is widely expressed in immune response cells. It is involved in both cancer development and progression as well as viral infection, notably by HIV-1. A variety of methods, including structural information, have suggested that the receptor may exist as a dimer or an oligomer. However, the mechanistic details surrounding receptor oligomerization and its potential dynamic regulation remain unclear. Using both biochemical and biophysical means, we confirm that CXCR4 can exist as a mixture of monomers, dimers, and higher-order oligomers in cell membranes and show that oligomeric structure becomes more complex as receptor expression levels increase. Mutations of CXCR4 residues located at a putative dimerization int

SUBMITTER: Ward RJ 

PROVIDER: S-EPMC7949023 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature